Disruption of the hslU gene, which encodes an ATPase subunit of the eukaryotic 26S proteasome homolog in Escherichia coli, suppresses the temperature-sensitive dnaA46 mutation

Tsutomu Katayama, Toshio Kubota, Makoto Takata, Nobuyoshi Akimitsu, Kazuhisa Sekimizu

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

The Escherichia coil hslVU genes encode subunits of an ATP-dependent protease, a homolog of the eukaryotic 265 proteasome. We found that the hslU gene is required for the temperature (40°C)-sensitive phenotype of the dnaA46 mutant, while other soluble ATP-dependent proteases, La (Lon) and Ti (Clp), were unrelated to this dnaA46 phenotype. Disruption of the hslU gene inhibited cell growth at high temperatures. These observations suggest a specific in vivo role for HslVU protease in denatured proteins. As the absence of HslU produces minicells in M9 medium, the protease may be involved in the cell cycle regulation.

Original languageEnglish
Pages (from-to)219-224
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume229
Issue number1
DOIs
Publication statusPublished - Dec 4 1996

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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